Dr. Paul Thompson lab publishes paper in Biochemistry

Dr. Paul Thompson lab published “Calcium Regulates the Nuclear Localization of Protein Arginine Deiminase 2.” in Biochemistry with Dr. Li Zheng and a team of collaborators.

The manuscript is about the Thompson Lab’s study showing that calcium regulates PAD2 transport into the nucleus. Protein arginine deiminases (PADs) are calcium-dependent enzymes that mediate the post-translational conversion of protein arginine into citrulline. Dysregulated PAD activity is associated with breast cancer in part via its ability to modify the architecture of chromatin and drive the transcription of estrogen receptor target genes.  Since PAD2 lacks a canonical nuclear localization sequence, how this enzyme is transported into the nucleus to modify chromatin associated proteins has long been a mystery.  This work by Dr. Zheng from the Thompson lab, provides the first insights into the transport of PAD2 into the nucleus. Using BioID2, a proximity-dependent biotinylation method for identifying interacting proteins, Dr. Zheng established that calcium binding to PAD2 weakens its association with ANXA5 in the cytoplasm and generates a pool of calcium-bound PAD2 that can interact with Ran. It is hypothesized that this latter interaction promotes the translocation of PAD2 into the nucleus. The findings in this work highlight a critical role for ANXA5 in regulating PAD2 and identify an unusual transit mechanism whereby proteins move between the cytosol and nucleus.

PMID:  31243954

Read the full article: https://pubs.acs.org/doi/10.1021/acs.biochem.9b00225
 
For more about the Thompson lab, please visit https://www.umassmed.edu/thompson

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